REMARK 2 REMARK 2 RESOLUTION. 1.66 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.9.2 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK, REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.55 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 65066 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.1713 REMARK 3 R VALUE (WORKING SET) : 0.1699 REMARK 3 FREE R VALUE : 0.1975 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.07 REMARK 3 FREE R VALUE TEST SET COUNT : 3299 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.70 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4557 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2221 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4330 REMARK 3 BIN R VALUE (WORKING SET) : 0.2211 REMARK 3 BIN FREE R VALUE : 0.2415 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.98 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 227 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3995 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 18 REMARK 3 SOLVENT ATOMS : 649 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 26.94 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.98 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.1960 REMARK 3 B22 (A**2) : -0.1342 REMARK 3 B33 (A**2) : -0.0617 REMARK 3 B12 (A**2) : 0.0833 REMARK 3 B13 (A**2) : 0.4088 REMARK 3 B23 (A**2) : -0.1996 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.199 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.9662 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.9574 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 4103 ; 2.00 ; HARMONIC REMARK 3 BOND ANGLES : 5579 ; 2.00 ; HARMONIC REMARK 3 TORSION ANGLES : 1355 ; 2.00 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 89 ; 2.00 ; HARMONIC REMARK 3 GENERAL PLANES : 589 ; 5.00 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 4103 ; 20.00 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 555 ; 5.00 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 5061 ; 4.00 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.011 REMARK 3 BOND ANGLES (DEGREES) : 1.10 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.93 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.84 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN C AND RESID 298-371) REMARK 3 ORIGIN FOR THE GROUP (A): 14.3769 -1.8033 -35.4087 REMARK 3 T TENSOR REMARK 3 T11: -0.0202 T22: -0.0626 REMARK 3 T33: -0.0303 T12: -0.0025 REMARK 3 T13: -0.0198 T23: 0.0016 REMARK 3 L TENSOR REMARK 3 L11: 1.9448 L22: 2.0002 REMARK 3 L33: 1.3966 L12: 0.8823 REMARK 3 L13: -0.1690 L23: -0.0633 REMARK 3 S TENSOR REMARK 3 S11: -0.0453 S12: 0.0300 S13: -0.0750 REMARK 3 S21: 0.0108 S22: 0.0238 S23: -0.1575 REMARK 3 S31: 0.0451 S32: 0.0717 S33: 0.0215 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN C AND RESID 372-395) REMARK 3 ORIGIN FOR THE GROUP (A): 7.6224 -7.9688 -42.3528 REMARK 3 T TENSOR REMARK 3 T11: -0.0205 T22: -0.0226 REMARK 3 T33: 0.0079 T12: -0.0188 REMARK 3 T13: -0.0171 T23: -0.0210 REMARK 3 L TENSOR REMARK 3 L11: -0.3659 L22: 3.5458 REMARK 3 L33: 0.9053 L12: 1.9287 REMARK 3 L13: -0.2349 L23: 0.4689 REMARK 3 S TENSOR REMARK 3 S11: 0.0070 S12: 0.0114 S13: -0.0332 REMARK 3 S21: -0.0900 S22: -0.0613 S23: 0.0196 REMARK 3 S31: -0.0193 S32: -0.0289 S33: 0.0543 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN H AND RESID 1-115) REMARK 3 ORIGIN FOR THE GROUP (A): 3.0529 -3.1697 -11.3016 REMARK 3 T TENSOR REMARK 3 T11: 0.0634 T22: -0.0684 REMARK 3 T33: -0.1228 T12: -0.0054 REMARK 3 T13: 0.0499 T23: 0.0337 REMARK 3 L TENSOR REMARK 3 L11: 1.3814 L22: 0.9897 REMARK 3 L33: 3.6791 L12: -0.7282 REMARK 3 L13: 0.2564 L23: 0.6990 REMARK 3 S TENSOR REMARK 3 S11: -0.2088 S12: -0.2495 S13: -0.1665 REMARK 3 S21: 0.2993 S22: 0.0841 S23: 0.1156 REMARK 3 S31: 0.5907 S32: -0.3089 S33: 0.1248 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN H AND RESID 116-216) REMARK 3 ORIGIN FOR THE GROUP (A): 1.2268 16.7124 18.7615 REMARK 3 T TENSOR REMARK 3 T11: -0.0300 T22: -0.0271 REMARK 3 T33: 0.0078 T12: -0.0130 REMARK 3 T13: 0.0233 T23: -0.0025 REMARK 3 L TENSOR REMARK 3 L11: 1.3079 L22: 1.5688 REMARK 3 L33: 0.5275 L12: -1.0621 REMARK 3 L13: 0.0046 L23: 0.1866 REMARK 3 S TENSOR REMARK 3 S11: 0.0344 S12: -0.0589 S13: 0.0674 REMARK 3 S21: 0.0118 S22: -0.0404 S23: -0.0084 REMARK 3 S31: 0.0378 S32: -0.0106 S33: 0.0060 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN L AND RESID 1-105) REMARK 3 ORIGIN FOR THE GROUP (A): -5.6805 15.4651 -18.1647 REMARK 3 T TENSOR REMARK 3 T11: -0.0565 T22: 0.0297 REMARK 3 T33: -0.0503 T12: 0.0515 REMARK 3 T13: -0.0353 T23: -0.0557 REMARK 3 L TENSOR REMARK 3 L11: 1.5930 L22: 1.7766 REMARK 3 L33: 0.9585 L12: -1.0808 REMARK 3 L13: -0.0965 L23: 0.9321 REMARK 3 S TENSOR REMARK 3 S11: -0.0829 S12: -0.2433 S13: 0.2015 REMARK 3 S21: -0.0120 S22: -0.0384 S23: 0.0818 REMARK 3 S31: -0.0463 S32: -0.3253 S33: 0.1213 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN L AND RESID 106-213) REMARK 3 ORIGIN FOR THE GROUP (A): 9.0487 29.2287 12.2527 REMARK 3 T TENSOR REMARK 3 T11: -0.0369 T22: -0.0357 REMARK 3 T33: -0.0056 T12: -0.0137 REMARK 3 T13: 0.0210 T23: 0.0115 REMARK 3 L TENSOR REMARK 3 L11: 2.0879 L22: 0.5218 REMARK 3 L33: 1.0989 L12: 0.1523 REMARK 3 L13: 0.9013 L23: 0.6388 REMARK 3 S TENSOR REMARK 3 S11: -0.0167 S12: 0.0996 S13: -0.0236 REMARK 3 S21: -0.1280 S22: 0.0169 S23: -0.0203 REMARK 3 S31: -0.1282 S32: 0.0131 S33: -0.0001 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP. REMARK 3 ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY REMARK 4 REMARK 4 4AL8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-MAR-12. REMARK 100 THE PDBE ID CODE IS EBI-51492. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I04 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.975 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79666 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.55 REMARK 200 RESOLUTION RANGE LOW (A) : 50.00 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0 REMARK 200 DATA REDUNDANCY : 7.1 REMARK 200 R MERGE (I) : 0.06 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 39.70 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0 REMARK 200 DATA REDUNDANCY IN SHELL : 3.9 REMARK 200 R MERGE FOR SHELL (I) : 0.49 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.30 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5490 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 29460 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 LYS C 295 REMARK 465 GLY C 296 REMARK 465 MET C 297 REMARK 465 CYS H 132 REMARK 465 GLY H 133 REMARK 465 ASP H 134 REMARK 465 THR H 135 REMARK 465 ARG H 217 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH L 2172 O HOH H 2240 2.10 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER H 85 67.81 39.71 REMARK 500 ALA H 103 -170.89 67.74 REMARK 500 SER H 153 88.25 -164.21 REMARK 500 SER H 164 -30.21 -136.62 REMARK 500 ARG L 30 -113.22 58.18 REMARK 500 ALA L 51 -39.95 72.62 REMARK 500 ALA L 84 -177.42 -170.81 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H1217 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H1218 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L1214 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4ALA RELATED DB: PDB REMARK 900 STRUCTURE OF DENGUE VIRUS DIII IN COMPLEX WITH FAB REMARK 900 2H12 REMARK 900 RELATED ID: 4AM0 RELATED DB: PDB REMARK 900 STRUCTURE OF DENGUE VIRUS STRAIN 4 DIII IN COMPLEX REMARK 900 WITH FAB 2H12